Research workbench
Crystal structure of the PRP38-MFAP1 complex of homo sapiens
Analyse Crystal structure of the PRP38-MFAP1 complex of homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F5S
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pre-mRNA-splicing factor 38A; Microfibrillar-associated protein 1
- UniProt
- Q8NAV1, P55081
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing factor 38A | protein | 177 | 54% helix, 12% strand | Q8NAV1 |
| B | Microfibrillar-associated protein 1 | protein | 53 | 92% helix, 0% strand | P55081 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.54 | 0.81 | 23 | empty |
| 2 | 81 | 0.39 | 0.78 | 17 | empty |
| 3 | 53 | 0.31 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 718 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5F5S · Crystal structure of the Prp38-MFAP1 complex of Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NAV1 · AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor 38A (Q8NAV1) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P55081 · AlphaFold monomer V2.0 prediction for microfibrillar-associated protein 1 (P55081) · a predicted model of the same protein · chain B against A, TM-score 0.83
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8NAV1
- Every structure of UniProt P55081
- Elsewhere: RCSB PDB 5F5S · PDBe 5F5S · UniProt Q8NAV1 · UniProt P55081
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